Crystal structure of Hsp33 chaperone (TM1394) from Thermotoga maritima at 2.20 Å resolution-Reference-Cited by-同舟云学术

Crystal structure of Hsp33 chaperone (TM1394) from Thermotoga maritima at 2.20 Å resolution

Published:2005-09-15 Issue:3 Volume:61 Page:669-673
ISSN:0887-3585
Container-title:Proteins: Structure, Function, and Bioinformatics
language:en
Short-container-title:Proteins

Author:

Jaroszewski Lukasz,Schwarzenbacher Robert,McMullan Daniel,Abdubek Polat,Agarwalla Sanjay,Ambing Eileen,Axelrod Herbert,Biorac Tanya,Canaves Jaume M.,Chiu Hsiu-Ju,Deacon Ashley M.,DiDonato Michael,Elsliger Marc-André,Godzik Adam,Grittini Carina,Grzechnik Slawomir K.,Hale Joanna,Hampton Eric,Han Gye Won,Haugen Justin,Hornsby Michael,Klock Heath E.,Koesema Eric,Kreusch Andreas,Kuhn Peter,Lesley Scott A.,Miller Mitchell D.,Moy Kin,Nigoghossian Edward,Paulsen Jessica,Quijano Kevin,Reyes Ron,Rife Chris,Spraggon Glen,Stevens Raymond C.,van den Bedem Henry,Velasquez Jeff,Vincent Juli,White Aprilfawn,Wolf Guenter,Xu Qingping,Hodgson Keith O.,Wooley John,Wilson Ian A.

Publisher

Wiley

Subject

Molecular Biology,Biochemistry,Structural Biology

Reference16 articles.

1. The 2.2 Å crystal structure of Hsp33: a heat shock protein with redox-regulated chaperone activity;Vijayalakshmi;Structure,2001

2. Chaperone activity with a redox switch;Jakob;Cell,1999

3. Activation of the redox-regulated chaperone Hsp33 by domain unfolding;Graf;J Biol Chem,2004

4. Structural genomics of the Thermotoga maritima proteome implemented in a high-throughput structure determination pipeline;Lesley;Proc Natl Acad Sci USA,2002

5. An approach to rapid protein crystallization using nanodroplets;Santarsiero;J Appl Crystallogr,2002

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